Marburg virus inclusions: A virus-induced microcompartment and interface to multivesicular bodies and the late endosomal compartment

Filovirus infection of target cells leads to the formation of virally induced cytoplasmic inclusions that contain viral nucleocapsids at different stages of maturation. While the role of the inclusions has been unclear since the identification of Marburg and Ebola viruses, it recently became clear t...

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Bibliographic Details
Published in:European journal of cell biology Vol. 94; no. 7-9; pp. 323 - 331
Main Authors: Dolnik, Olga, Stevermann, Lea, Kolesnikova, Larissa, Becker, Stephan
Format: Journal Article
Language:English
Published: Germany Elsevier GmbH 01.07.2015
Subjects:
Alix
Animals
Cell Compartmentation - physiology
Cell Line
DNA-Binding Proteins - metabolism
Endosomal Sorting Complexes Required for Transport - metabolism
Endosomes - metabolism
ESCRT
Humans
Inclusion Bodies, Viral - metabolism
Inclusions
Lamp-1
Late domain
Lysosomal Membrane Proteins - metabolism
Macrophages - virology
Marburg virus
Marburg Virus Disease - virology
Marburgvirus - growth & development
Multivesicular Bodies - physiology
Nedd4
Nucleocapsid - biosynthesis
Nucleocapsid - metabolism
Nucleoprotein
Nucleoproteins - metabolism
Protein Transport
Pseudopodia - metabolism
ras GTPase-Activating Proteins - metabolism
Transcription Factors - metabolism
Virus Release - physiology
Virus Replication - physiology
Late domain
Marburg virus
ESCRT
Alix
Lamp-1
Nedd4
Nucleoprotein
Inclusions
ISSN:0171-9335, 1618-1298, 1618-1298
Online Access:Get full text
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Summary:Filovirus infection of target cells leads to the formation of virally induced cytoplasmic inclusions that contain viral nucleocapsids at different stages of maturation. While the role of the inclusions has been unclear since the identification of Marburg and Ebola viruses, it recently became clear that the inclusions are the sites of viral replication, nucleocapsid formation and maturation. Live cell imaging analyses revealed that mature nucleocapsids are transported from inclusions to the filopodia, which represent the major budding sites. Moreover, inclusions recruit cellular proteins that have been shown to support the transport of nucleocapsids. For example, the tumor susceptibility gene 101 protein (Tsg101) interacts with a late domain motif in the nucleocapsid protein NP and recruits the actin-nucleation factor IQGAP1. Complexes of nucleocapsids together with Tsg101 and IQGAP1 are then co-transported along actin filaments. We detected additional proteins (Alix, Nedd4 and the AAA-type ATPase VPS4) of the endosomal sorting complex required for transport (ESCRT) that are recruited into inclusions. Together, the results suggest that nucleocapsids recruit the machinery that enhances viral budding at the plasma membrane. Furthermore, we identified Lamp1 as a marker of the late endosomal compartment in inclusions, while ER, Golgi, TGN and early endosomal markers were absent. In addition, we observed that LC3, a marker of autophagosomal membranes, was present in inclusions. The 3D structures of inclusions show an intricate structure that seems to accommodate an intimate cooperation between cellular and viral components with the intention to support viral transport and budding.
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ISSN:0171-9335
1618-1298
1618-1298
DOI:10.1016/j.ejcb.2015.05.006